4mb1

X-ray diffraction
1.4Å resolution

The Structure of MalL mutant enzyme G202P from Bacillus subtilus

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-126554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oligo-1,6-glucosidase 1 Chain: A
Molecule details ›
Chain: A
Length: 561 amino acids
Theoretical weight: 66.2 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O06994 (Residues: 1-561; Coverage: 100%)
Gene names: BSU34560, malL, yvdL
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P21
Unit cell:
a: 48.5Å b: 101.07Å c: 61.85Å
α: 90° β: 112.86° γ: 90°
R-values:
R R work R free
0.174 0.173 0.2
Expression system: Escherichia coli BL21(DE3)